Abstract
Molecular properties of the two isozymes expressed by the B allele at the red cell acid phosphatase locus (ACP1) have been studied to distinguish between possible mechanisms for their production. The difference in electric charge exhibited by the native isozymes was retained under denaturing conditions; the unfolded peptide chains renatured without conversion of one form to the other. Chromatographic analysis [thin-layer chromatography (TLC) and high-performance liquid chromatography (HPLC)] of tryptic digests showed 12 peptides common to both isozymes but also revealed 5 peptides unique to one isozyme and 3 (possibly 4) peptides unique to the other. These findings argue against both conformational isomerization and simple posttranslational modification as the mechanism of generation of the two isozymes. We suggest that the two isozymes are synthesized as discrete molecular entities.
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This work was supported by a grant from “Statens Lægevidenskabelige Forskningsråd,” Copenhagen, and a faculty research grant, University of California.
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Dissing, J., Sensabaugh, G.F. Human red cell acid phosphatase (ACP1): Evidence for differences in the primary structure of the two isozymes encoded by the ACP1*B allele. Biochem Genet 25, 919–927 (1987). https://doi.org/10.1007/BF00502610
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DOI: https://doi.org/10.1007/BF00502610